Cargando…
Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli
Being an essential multifunctional platform and interface to the extracellular environment, the cell membrane constitutes a valuable target for the modification and manipulation of cells and cellular behavior, as well as for the implementation of artificial, new-to-nature functionality. While bacter...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10619624/ https://www.ncbi.nlm.nih.gov/pubmed/37920346 http://dx.doi.org/10.1039/d3sc02960c |
_version_ | 1785130026075684864 |
---|---|
author | Wegner, Tristan Dombovski, Alexander Gesing, Katrin Köhrer, Alexander Elinkmann, Matthias Karst, Uwe Glorius, Frank Jose, Joachim |
author_facet | Wegner, Tristan Dombovski, Alexander Gesing, Katrin Köhrer, Alexander Elinkmann, Matthias Karst, Uwe Glorius, Frank Jose, Joachim |
author_sort | Wegner, Tristan |
collection | PubMed |
description | Being an essential multifunctional platform and interface to the extracellular environment, the cell membrane constitutes a valuable target for the modification and manipulation of cells and cellular behavior, as well as for the implementation of artificial, new-to-nature functionality. While bacterial cell surface functionalization via expression and presentation of recombinant proteins has extensively been applied, the corresponding application of functionalizable lipid mimetics has only rarely been reported. Herein, we describe an approach to equip E. coli cells with a lipid-mimicking, readily membrane-integrating imidazolium salt and a corresponding NHC–palladium complex that allows for flexible bacterial membrane surface functionalization and enables E. coli cells to perform cleavage of propargyl ethers present in the surrounding cell medium. We show that this approach can be combined with already established on-surface functionalization, such as bacterial surface display of enzymes, i.e. laccases, leading to a new type of cascade reaction. Overall, we envision the herein presented proof-of-concept studies to lay the foundation for a multifunctional toolbox that allows flexible and broadly applicable functionalization of bacterial membranes. |
format | Online Article Text |
id | pubmed-10619624 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-106196242023-11-02 Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli Wegner, Tristan Dombovski, Alexander Gesing, Katrin Köhrer, Alexander Elinkmann, Matthias Karst, Uwe Glorius, Frank Jose, Joachim Chem Sci Chemistry Being an essential multifunctional platform and interface to the extracellular environment, the cell membrane constitutes a valuable target for the modification and manipulation of cells and cellular behavior, as well as for the implementation of artificial, new-to-nature functionality. While bacterial cell surface functionalization via expression and presentation of recombinant proteins has extensively been applied, the corresponding application of functionalizable lipid mimetics has only rarely been reported. Herein, we describe an approach to equip E. coli cells with a lipid-mimicking, readily membrane-integrating imidazolium salt and a corresponding NHC–palladium complex that allows for flexible bacterial membrane surface functionalization and enables E. coli cells to perform cleavage of propargyl ethers present in the surrounding cell medium. We show that this approach can be combined with already established on-surface functionalization, such as bacterial surface display of enzymes, i.e. laccases, leading to a new type of cascade reaction. Overall, we envision the herein presented proof-of-concept studies to lay the foundation for a multifunctional toolbox that allows flexible and broadly applicable functionalization of bacterial membranes. The Royal Society of Chemistry 2023-10-06 /pmc/articles/PMC10619624/ /pubmed/37920346 http://dx.doi.org/10.1039/d3sc02960c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Wegner, Tristan Dombovski, Alexander Gesing, Katrin Köhrer, Alexander Elinkmann, Matthias Karst, Uwe Glorius, Frank Jose, Joachim Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli |
title | Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli |
title_full | Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli |
title_fullStr | Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli |
title_full_unstemmed | Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli |
title_short | Combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of E. coli |
title_sort | combining lipid-mimicking-enabled transition metal and enzyme-mediated catalysis at the cell surface of e. coli |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10619624/ https://www.ncbi.nlm.nih.gov/pubmed/37920346 http://dx.doi.org/10.1039/d3sc02960c |
work_keys_str_mv | AT wegnertristan combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT dombovskialexander combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT gesingkatrin combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT kohreralexander combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT elinkmannmatthias combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT karstuwe combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT gloriusfrank combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli AT josejoachim combininglipidmimickingenabledtransitionmetalandenzymemediatedcatalysisatthecellsurfaceofecoli |